ID   U4K819_9VIBR            Unreviewed;       289 AA.
AC   U4K819;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative N-acetylneuraminate lyase {ECO:0000313|EMBL:CCO58784.1};
DE            EC=4.1.3.3 {ECO:0000313|EMBL:CCO58784.1};
GN   ORFNames=VIBNI_A2737 {ECO:0000313|EMBL:CCO58784.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO58784.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO58784.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA   Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT   identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
CC   -!- SIMILARITY: Belongs to the DapA family.
CC       {ECO:0000256|PIRNR:PIRNR001365}.
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DR   EMBL; FO203526; CCO58784.1; -; Genomic_DNA.
DR   RefSeq; WP_022551430.1; NC_022528.1.
DR   AlphaFoldDB; U4K819; -.
DR   STRING; 28173.VIBNI_A2737; -.
DR   KEGG; vni:VIBNI_A2737; -.
DR   PATRIC; fig|1260221.3.peg.2606; -.
DR   eggNOG; COG0329; Bacteria.
DR   OrthoDB; 199953at2; -.
DR   Proteomes; UP000016895; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; DapA-like.
DR   InterPro; IPR020625; Schiff_base-form_aldolases_AS.
DR   PANTHER; PTHR42849; N-ACETYLNEURAMINATE LYASE; 1.
DR   PANTHER; PTHR42849:SF1; N-ACETYLNEURAMINATE LYASE; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PIRSF; PIRSF001365; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   SMART; SM01130; DHDPS; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00666; DHDPS_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001365};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270}.
FT   ACT_SITE        132
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   ACT_SITE        160
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-1"
FT   BINDING         201
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001365-2"
SQ   SEQUENCE   289 AA;  32669 MW;  6A53A18417BE8603 CRC64;
     MEGIFVPLMT PFSADGELEY SKLDAMIEYH ISQGVHGFYV GGSSSECFMM SISERQKVLK
     YVSQVVKKRV PVIAHVGAIA LTDVRLLIDT ALDENYDVIS AIPPFYYGFT KQEVTYYYQS
     ILDYTDLPLL LYNIPGTTGV TFTHETLLNL LMMDNIIGIK HTTPDMFFIE RLRHLQQDSL
     IFHGEDSMLV NGLQMGASGG IGTTYNLMPA QYVKLFEAMK QGDVDKAMAL QHQVNRVTEV
     LLEVGLYQSI KFAMSEMGID YGHCREPFLP LSKEDKGRVM TCLERYGYL
//